1NHP
CRYSTALLOGRAPHIC ANALYSES OF NADH PEROXIDASE CYS42ALA AND CYS42SER MUTANTS: ACTIVE SITE STRUCTURE, MECHANISTIC IMPLICATIONS, AND AN UNUSUAL ENVIRONMENT OF ARG303
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | NADH PEROXIDASE | polymer | 447 | 49571.2 | 1 | UniProt (P37062) Pfam (PF00070) Pfam (PF02852) | Enterococcus faecalis | |
| 2 | B, C (A) | SULFATE ION | non-polymer | 96.1 | 2 | Chemie (SO4) | |||
| 3 | D (A) | FLAVIN-ADENINE DINUCLEOTIDE | non-polymer | 785.5 | 1 | Chemie (FAD) | |||
| 4 | E (A) | water | water | 18.0 | 243 | Chemie (HOH) |
Sequence modifications
A: 1 - 447 (UniProt: P37062)
| PDB | External Database | Details |
|---|---|---|
| Ala 42 | Cys 42 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 49571.2 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 977.7 | |
| All* | Total formula weight | 50548.8 |
